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Title: Prion-like Misfolding and Vasicular Spread of Toxic Proteins in Neurodegenerative DiseasesAuthors: Edward Pokrishevsky, Judith M. Silverman and Neil R. Cashman*Affiliation: Brain Research Centre, The University of British Columbia, 2211 Wesbrook Mall, Vancouver, BC V6T2B5, Canada (Neil.Cashman@vch.ca)Abstract: Prion diseases, such as Creutzfeldt–Jakob disease, have been traditionally considered to be caused by a separate class of infectious agents. The pathologically misfolded prion protein can catalyze the conversion of its natively folded counterpart into the toxic form; therefore forming a recruiting seed for protein misfolding that may spread intercellularly until the entire tissue is infected. The transmission is thought to occur through an ongoing release and uptake of exosomes, small membranous vesicles used by both neurons and astrocytes for cell-to-cell communication. Recent discoveries expand the prion field, to include prion-like proteins implicated in other neurodegenerative diseases, including Alzheimer's, Parkinson's, Huntington's, amyotrophic lateral sclerosis, and the tauopathies. In addition to sustaining an intracellular recruitment, misfolding of prion-like proteins may also spread intercellularly, a process that is implied by the systematic spread of neurodegeneration. This pattern of infectivity suggests intercellular mechanisms of communications involving exosomes or continuous exchange of inclusions containing the disease specific infectious prion-like proteins. The goal of this review was twofold: to summarize the current state of knowledge of the prion-like proteins in neurodegenerative diseases and to examine their potential mechanisms of transmission. Keywords: neurodegenerative diseases; Alzheimer’s; Huntington’s; Parkinson’s; amyotrophic lateral sclerosis; prions; exosomes